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Structure Determination of Different Casein Components
Abstract Casein is the main protein component of milk. It is not a homogeneous polymer but consists of several types of casein, and forms large spherical micelles of remarkable stability. The reason for this stability is not yet fully understood. In co-operation with other laboratories, we have been able to obtain well-separated individual fractions which were studied with regard to their capability for micelle formation and the micelle structure. Studies have been carried out with the α, β and κ-caseins. Small-angle neutron scattering and combined static and dynamic light scattering have been applied, which gave information on the particle weight Mw, the radius of gyration Rg and the hydrodynamic radius RH, and on the particle scattering factor Pz(q), where q = (4π/λ) sin θ/2. The three caseins show strikingly different behaviour. For the β-casein, a star-like structure was detected which corresponds to the aggregation pattern of common soap micelles. The aggregation number is 38. The aggregates of κ-casein appear to be composed of star-like sub-micelles; each sub-micelle contains nine κ-casein molecules and the total aggregation number is 140. α-Casein forms long fibrils which resemble worm-like filaments. The contour length of the cylinders was found to be L ≃ 1600 nm, and the filaments appear to be composed of about 12 Kuhn segments of lK = 133 ± 12 nm in length.
Structure Determination of Different Casein Components
Abstract Casein is the main protein component of milk. It is not a homogeneous polymer but consists of several types of casein, and forms large spherical micelles of remarkable stability. The reason for this stability is not yet fully understood. In co-operation with other laboratories, we have been able to obtain well-separated individual fractions which were studied with regard to their capability for micelle formation and the micelle structure. Studies have been carried out with the α, β and κ-caseins. Small-angle neutron scattering and combined static and dynamic light scattering have been applied, which gave information on the particle weight Mw, the radius of gyration Rg and the hydrodynamic radius RH, and on the particle scattering factor Pz(q), where q = (4π/λ) sin θ/2. The three caseins show strikingly different behaviour. For the β-casein, a star-like structure was detected which corresponds to the aggregation pattern of common soap micelles. The aggregation number is 38. The aggregates of κ-casein appear to be composed of star-like sub-micelles; each sub-micelle contains nine κ-casein molecules and the total aggregation number is 140. α-Casein forms long fibrils which resemble worm-like filaments. The contour length of the cylinders was found to be L ≃ 1600 nm, and the filaments appear to be composed of about 12 Kuhn segments of lK = 133 ± 12 nm in length.
Structure Determination of Different Casein Components
Thurn, Angelika (author) / Burchard, Walther (author)
1988-01-01
17 pages
Article/Chapter (Book)
Electronic Resource
English
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